Photocontrolled Folding and Unfolding of a Collagen Triple Helix
✍ Scribed by Ulrike Kusebauch; Sergio A. Cadamuro; Hans-Jürgen Musiol; Martin O. Lenz; Josef Wachtveitl; Luis Moroder; Christian Renner
- Publisher
- John Wiley and Sons
- Year
- 2006
- Tongue
- English
- Weight
- 165 KB
- Volume
- 45
- Category
- Article
- ISSN
- 0044-8249
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Collagen is a ubiquitous biomaterial that forms the supporting structures in skin, bone, tendons, cartilage, and blood vessels. Numerous types of collagen have been identified, and the tertiary structure of each shares the common structural motif of the collagen triple helix (CTH). [1] The CTH motif
## Synopsis Variations I-XVIII of a trimerlike cross-linked collagen model peptide were synthesized and used to investigate the cooperation of different neighboring Gly-X-Y tripeptides. The carboxyterminal decapentapeptide of the triple-helical part of collagen type I was chosen as the starting po